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| Name: |
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Mitch McVey |
| Title: |
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Assistant Professor
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| Departmental Affiliation: |
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Biology Department
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| Degrees: |
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B.A. in Molecular, Cellular, and Developmental Biology, M.I.T.
2001, Ph.D. in Biology,
University of North Carolina at Chapel Hill
2002-2005, SPIRE postdoctoral fellowship |
| Expertise: |
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Molecular Biology and Genetics: DNA repair and recombination in Drosophila, genomic instability and its relationship to aging.
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| Major Awards: |
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New Scholar Award in Aging,
Ellison Medical Foundation, 2006-2010 |
| E-mail: |
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mitch.mcvey@tufts.edu
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| Other websites: |
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http://ase.tufts.edu/biology/faculty/mcvey
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| Scholarship & Research: |
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The McVey laboratory studies molecular mechanisms of DNA repair and recombination using Drosophila melanogaster as a model system. Many inherited diseases in humans are caused by mutations in genes involved in DNA repair pathways. One example of this involves the RecQ family of DNA helicases, of which there are five members in mammals. Single mutations in three of the members, WRN, BLM, and RECQ4, result in clinically distinct disorders that are characterized by genome instability and a predisposition to cancer. Both biochemical and genetic data suggest that the RecQ helicases are involved in DNA repair and recombination, although their precise functions are not fully defined. Drosophila has four RecQ orthologues. Using gene targeting and molecular genetic assays, we are currently investigating the functions of these Drosophila RecQ helicases.
Another interest of the lab addresses the question of how cells choose between different DNA repair pathways to fix a DNA double-strand break. Previous research has demonstrated that, in flies, double-strand breaks are preferentially repaired using homologous recombination, resulting in error-free repair of the break. If this primary pathway is blocked, then the break is repaired by an error-prone non-homologous end-joining mechanism. Surprisingly, end-joining repair of a P-element induced double-strand break in flies is largely independent of the DNA ligase IV protein, which plays a central role in end joining in both yeast and mammals. We are currently characterizing the genetic requirements for this aberrant end-joining pathway. Further details and additional research interests can be found on the lab website.
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